The 1.05w refinement of the DNA-binding domain of the Heat Shock Transcription Factor (HSF) has been recently been completed. Data were collected on two frozen crystals using beamline 7-1. The program SHELXL was used to refine the 92 amino acid proteins, starting with the 1.8 w refined model of this helix-turn-helix variant. Included in the refinement was a six-parameter individual anisotropic B-factor refinement for all protein and solvent atoms. The refinement was continued until all reasonable difference Fourier peaks could be accounted for, and nearly all discrete disorder was modeled satisfactorily. Ten side chains were modeled with alternate conformations. Despite the high resolution data, however, an area of extreme disorder that encompassed four amino acids could not be modeled. There was one area of main chain disorder that could not be modeled. At this resolution, a nearly complete set of primary solvent and ion molecules could be modeled, including 149 waters in full and partial occupancy. Two newly revealed features include a molecule of trifluoroacetic acid bound in a hydrophobic pocket and a network of waters supporting a helix that is distorted by an a-helical bulge and a proline-induced kink.